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Protein

Spindlin-1

Gene

SPIN1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Chromatin reader that specifically recognizes and binds histone H3 both trimethylated at 'Lys-4' and asymmetrically dimethylated at 'Arg-8' (H3K4me3 and H3R8me2a) and acts as an activator of Wnt signaling pathway downstream of PRMT2. In case of cancer, promotes cell cancer proliferation via activation of the Wnt signaling pathway (PubMed:24589551). Overexpression induces metaphase arrest and chromosomal instability. Localizes to active rDNA loci and promotes the expression of rRNA genes (PubMed:21960006). May play a role in cell-cycle regulation during the transition from gamete to embryo. Involved in oocyte meiotic resumption, a process that takes place before ovulation to resume meiosis of oocytes blocked in prophase I: may act by regulating maternal transcripts to control meiotic resumption.3 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei173Histone H3K4me3 and H3R8me2a1
Binding sitei180Histone H3K4me3 and H3R8me2a1
Binding sitei184Histone H3K4me3 and H3R8me2a1

GO - Molecular functioni

  • methylated histone binding Source: UniProtKB

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Chromatin regulator, Developmental protein

Keywords - Biological processi

Cell cycle, Meiosis, Wnt signaling pathway

Names & Taxonomyi

Protein namesi
Recommended name:
Spindlin-1
Alternative name(s):
Ovarian cancer-related protein
Spindlin1
Gene namesi
Name:SPIN1
Synonyms:OCR, SPIN
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 9

Organism-specific databases

HGNCiHGNC:11243. SPIN1.

Subcellular locationi

GO - Cellular componenti

  • nucleolus Source: UniProtKB
  • nucleus Source: LIFEdb
  • spindle Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi72W → A or R: Impaired binding to histone H3K4me3 and H3R8me2a and impaired ability to activate the Wnt signaling pathway. 1 Publication1
Mutagenesisi98Y → R: Impaired binding to histone H3K4me3 and H3R8me2a and impaired ability to activate the Wnt signaling pathway. 1 Publication1
Mutagenesisi109S → A: Impaired phosphorylation. 1 Publication1
Mutagenesisi124S → A: Impaired phosphorylation. 1 Publication1
Mutagenesisi141F → A: Impaired binding to histone H3K4me3 and H3R8me2a and impaired ability to activate the Wnt signaling pathway. Impaired ability to activate expression of pre-rRNA. 2 Publications1
Mutagenesisi142E → A: Impaired binding to histone H3K4me3 and H3R8me2a. 1 Publication1
Mutagenesisi170Y → A: Impaired binding to histone H3K4me3 and H3R8me2a and impaired ability to activate the Wnt signaling pathway. Impaired ability to activate expression of pre-rRNA. 2 Publications1
Mutagenesisi177Y → A: Impaired binding to histone H3K4me3 and H3R8me2a. 1 Publication1
Mutagenesisi184D → A or R: Impaired binding to histone H3K4me3 and H3R8me2a. 2 Publications1
Mutagenesisi189D → A or R: Impaired binding to histone H3K4me3. 1 Publication1
Mutagenesisi251F → R: Impaired binding to histone H3K4me3 and H3R8me2a and impaired ability to activate the Wnt signaling pathway. 1 Publication1

Organism-specific databases

DisGeNETi10927.
OpenTargetsiENSG00000106723.
PharmGKBiPA162404504.

Polymorphism and mutation databases

BioMutaiSPIN1.
DMDMi93141317.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001813671 – 262Spindlin-1Add BLAST262

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei44N6-acetyllysineBy similarity1
Modified residuei109Phosphoserine; by AURKA1 Publication1
Modified residuei124Phosphoserine; by AURKACombined sources1 Publication1
Modified residuei199PhosphoserineCombined sources1

Post-translational modificationi

Phosphorylated during oocyte meiotic maturation.By similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiQ9Y657.
MaxQBiQ9Y657.
PaxDbiQ9Y657.
PeptideAtlasiQ9Y657.
PRIDEiQ9Y657.

PTM databases

iPTMnetiQ9Y657.
PhosphoSitePlusiQ9Y657.

Expressioni

Tissue specificityi

Highly expressed in ovarian cancer tissues.1 Publication

Gene expression databases

BgeeiENSG00000106723.
CleanExiHS_SPIN1.
ExpressionAtlasiQ9Y657. baseline and differential.
GenevisibleiQ9Y657. HS.

Organism-specific databases

HPAiHPA000162.

Interactioni

Subunit structurei

Homodimer; may form higher-order oligomers (PubMed:17082182). Interacts with TCF7L2/TCF4; the interaction is direct. Interacts with HABP4 and SERBP1.4 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
HSPB1P047922EBI-727129,EBI-352682

GO - Molecular functioni

  • methylated histone binding Source: UniProtKB

Protein-protein interaction databases

BioGridi116130. 33 interactors.
DIPiDIP-40062N.
IntActiQ9Y657. 8 interactors.
MINTiMINT-1428826.
STRINGi9606.ENSP00000365019.

Structurei

Secondary structure

1262
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi56 – 62Combined sources7
Beta strandi65 – 67Combined sources3
Beta strandi70 – 79Combined sources10
Beta strandi87 – 91Combined sources5
Beta strandi98 – 100Combined sources3
Turni102 – 104Combined sources3
Beta strandi108 – 117Combined sources10
Helixi126 – 132Combined sources7
Beta strandi136 – 142Combined sources7
Beta strandi144 – 146Combined sources3
Beta strandi148 – 158Combined sources11
Beta strandi160 – 162Combined sources3
Beta strandi166 – 170Combined sources5
Beta strandi173 – 179Combined sources7
Helixi181 – 186Combined sources6
Beta strandi190 – 192Combined sources3
Beta strandi217 – 221Combined sources5
Turni223 – 225Combined sources3
Beta strandi227 – 235Combined sources9
Beta strandi237 – 239Combined sources3
Beta strandi242 – 247Combined sources6
Beta strandi254 – 257Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2NS2X-ray2.20A/B26-262[»]
4H75X-ray2.10A27-262[»]
4MZFX-ray2.10B50-262[»]
4MZGX-ray1.70B/D50-262[»]
4MZHX-ray2.20A50-262[»]
ProteinModelPortaliQ9Y657.
SMRiQ9Y657.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9Y657.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni53 – 116Tudor-like domain 1Add BLAST64
Regioni93 – 98Histone H3K4me3 and H3R8me2a binding6
Regioni132 – 193Tudor-like domain 2Add BLAST62
Regioni142Histone H3K4me3 and H3R8me2a binding1
Regioni213 – 262Tudor-like domain 3Add BLAST50
Regioni250 – 252Histone H3K4me3 and H3R8me2a binding3

Domaini

The 3 tudor-like domains (also named Spin/Ssty repeats) specifically recognize and bind methylated histones (PubMed:23077255, PubMed:24589551). H3K4me3 and H3R8me2a are recognized by tudor-like domains 2 and 1, respectively (PubMed:24589551).3 Publications

Sequence similaritiesi

Belongs to the SPIN/STSY family.Curated

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiENOG410IGUH. Eukaryota.
ENOG410XQI2. LUCA.
GeneTreeiENSGT00760000119261.
HOGENOMiHOG000293367.
HOVERGENiHBG000686.
InParanoidiQ9Y657.
OMAiKHRSNVG.
OrthoDBiEOG091G0EE3.
PhylomeDBiQ9Y657.
TreeFamiTF332665.

Family and domain databases

InterProiIPR003671. SPIN/Ssty.
IPR029579. Spindlin-1/z.
[Graphical view]
PANTHERiPTHR10405. PTHR10405. 1 hit.
PTHR10405:SF15. PTHR10405:SF15. 1 hit.
PfamiPF02513. Spin-Ssty. 3 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9Y657-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKTPFGKTPG QRSRADAGHA GVSANMMKKR TSHKKHRSSV GPSKPVSQPR
60 70 80 90 100
RNIVGCRIQH GWKEGNGPVT QWKGTVLDQV PVNPSLYLIK YDGFDCVYGL
110 120 130 140 150
ELNKDERVSA LEVLPDRVAT SRISDAHLAD TMIGKAVEHM FETEDGSKDE
160 170 180 190 200
WRGMVLARAP VMNTWFYITY EKDPVLYMYQ LLDDYKEGDL RIMPDSNDSP
210 220 230 240 250
PAEREPGEVV DSLVGKQVEY AKEDGSKRTG MVIHQVEAKP SVYFIKFDDD
260
FHIYVYDLVK TS
Length:262
Mass (Da):29,601
Last modified:April 18, 2006 - v3
Checksum:i49F86CBCC7A0AA01
GO

Sequence cautioni

The sequence AAD43035 differs from that shown. Reason: Frameshift at position 21.Curated
The sequence AAG38112 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence AAG48367 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence CAB66653 differs from that shown. Reason: Erroneous termination at position 171. Translated as Glu.Curated
The sequence CAG38515 differs from that shown. Reason: Erroneous termination at position 171. Translated as Glu.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti49P → S in BAG52466 (PubMed:14702039).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_053690221A → P.Corresponds to variant rs34794905dbSNPEnsembl.1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF106682 mRNA. Translation: AAD43035.1. Frameshift.
AF087864 mRNA. Translation: AAG48367.1. Different initiation.
AF317228 mRNA. Translation: AAG38112.1. Different initiation.
AL136719 mRNA. Translation: CAB66653.1. Sequence problems.
BT007314 mRNA. Translation: AAP35978.1.
AK092017 mRNA. Translation: BAG52466.1.
AK289691 mRNA. Translation: BAF82380.1.
AK290009 mRNA. Translation: BAF82698.1.
AK315854 mRNA. Translation: BAF98745.1.
AL353748 Genomic DNA. Translation: CAH72406.1.
CH471089 Genomic DNA. Translation: EAW62753.1.
BC013571 mRNA. No translation available.
BC114515 mRNA. Translation: AAI14516.1.
BC114565 mRNA. Translation: AAI14566.1.
CR533484 mRNA. Translation: CAG38515.1. Sequence problems.
CCDSiCCDS43843.1.
RefSeqiNP_006708.2. NM_006717.2.
UniGeneiHs.146804.

Genome annotation databases

EnsembliENST00000375859; ENSP00000365019; ENSG00000106723.
GeneIDi10927.
KEGGihsa:10927.
UCSCiuc004apy.4. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF106682 mRNA. Translation: AAD43035.1. Frameshift.
AF087864 mRNA. Translation: AAG48367.1. Different initiation.
AF317228 mRNA. Translation: AAG38112.1. Different initiation.
AL136719 mRNA. Translation: CAB66653.1. Sequence problems.
BT007314 mRNA. Translation: AAP35978.1.
AK092017 mRNA. Translation: BAG52466.1.
AK289691 mRNA. Translation: BAF82380.1.
AK290009 mRNA. Translation: BAF82698.1.
AK315854 mRNA. Translation: BAF98745.1.
AL353748 Genomic DNA. Translation: CAH72406.1.
CH471089 Genomic DNA. Translation: EAW62753.1.
BC013571 mRNA. No translation available.
BC114515 mRNA. Translation: AAI14516.1.
BC114565 mRNA. Translation: AAI14566.1.
CR533484 mRNA. Translation: CAG38515.1. Sequence problems.
CCDSiCCDS43843.1.
RefSeqiNP_006708.2. NM_006717.2.
UniGeneiHs.146804.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2NS2X-ray2.20A/B26-262[»]
4H75X-ray2.10A27-262[»]
4MZFX-ray2.10B50-262[»]
4MZGX-ray1.70B/D50-262[»]
4MZHX-ray2.20A50-262[»]
ProteinModelPortaliQ9Y657.
SMRiQ9Y657.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi116130. 33 interactors.
DIPiDIP-40062N.
IntActiQ9Y657. 8 interactors.
MINTiMINT-1428826.
STRINGi9606.ENSP00000365019.

PTM databases

iPTMnetiQ9Y657.
PhosphoSitePlusiQ9Y657.

Polymorphism and mutation databases

BioMutaiSPIN1.
DMDMi93141317.

Proteomic databases

EPDiQ9Y657.
MaxQBiQ9Y657.
PaxDbiQ9Y657.
PeptideAtlasiQ9Y657.
PRIDEiQ9Y657.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000375859; ENSP00000365019; ENSG00000106723.
GeneIDi10927.
KEGGihsa:10927.
UCSCiuc004apy.4. human.

Organism-specific databases

CTDi10927.
DisGeNETi10927.
GeneCardsiSPIN1.
HGNCiHGNC:11243. SPIN1.
HPAiHPA000162.
MIMi609936. gene.
neXtProtiNX_Q9Y657.
OpenTargetsiENSG00000106723.
PharmGKBiPA162404504.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410IGUH. Eukaryota.
ENOG410XQI2. LUCA.
GeneTreeiENSGT00760000119261.
HOGENOMiHOG000293367.
HOVERGENiHBG000686.
InParanoidiQ9Y657.
OMAiKHRSNVG.
OrthoDBiEOG091G0EE3.
PhylomeDBiQ9Y657.
TreeFamiTF332665.

Miscellaneous databases

ChiTaRSiSPIN1. human.
EvolutionaryTraceiQ9Y657.
GeneWikiiSPIN1.
GenomeRNAii10927.
PROiQ9Y657.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000106723.
CleanExiHS_SPIN1.
ExpressionAtlasiQ9Y657. baseline and differential.
GenevisibleiQ9Y657. HS.

Family and domain databases

InterProiIPR003671. SPIN/Ssty.
IPR029579. Spindlin-1/z.
[Graphical view]
PANTHERiPTHR10405. PTHR10405. 1 hit.
PTHR10405:SF15. PTHR10405:SF15. 1 hit.
PfamiPF02513. Spin-Ssty. 3 hits.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiSPIN1_HUMAN
AccessioniPrimary (citable) accession number: Q9Y657
Secondary accession number(s): A8K0X6
, B3KRQ4, Q7KZJ8, Q9GZT2, Q9H0N7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 20, 2001
Last sequence update: April 18, 2006
Last modified: November 2, 2016
This is version 127 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 9
    Human chromosome 9: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.